A major focus in our laboratory is to reveal functional mechanisms of integral membrane proteins at the level of chemistry and atomic structure for impact on drug design. Membrane proteins include bacteriorhodopsin, halorhodopsin, AtCase-bacteriorhodopsin fusion protein, human potassium channel, serotonin receptor, CHIP 28 and MIP 26 (two water channels from red cell membranes and bovine lenses respectively), and thrombin receptor. Following expression in E. coli and H. halobium, these proteins will be purified and characterized prior to 3-D crystallization. To facilitate characterization and crystallization, mass spectrometry will be used to assay synthetic peptides for antibody production, assay protein purity and post-translational processing events, and to determine mass and purity of novel detergents including peptide-based 'peptitergents'. These collaborative efforts will develop procedures in purification of hydrophobic peptides and proteins in environments amenable for mass spectrometry.